Detail Information for IndEnz0002001732
IED ID IndEnz0002001732
Enzyme Type ID protease001732
Protein Name Capsid assembly scaffolding protein
Gene product 17
Gp17
Head morphogenesis protein
Scaffold protein

Cleaved into: Maturation protease
EC 3.4.21.-
Gene Name
Organism Haemophilus phage HP1 (strain HP1c1) (Bacteriophage HP1)
Taxonomic Lineage Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales Myoviridae (phages with contractile tails) Peduovirinae Hpunavirus Haemophilus phage HP1 (Bacteriophage HP1) Haemophilus phage HP1 (strain HP1c1) (Bacteriophage HP1)
Enzyme Sequence MNKSKLKTDFICIATSGYTVDGRQITAQELHEMAETYDPEHYTANLWPEHRRWFNMGQVIELKAEENEKGETQLFAIIAPNKELIEYNRAGQYLFTSIEITPNFRNSGKAYLSGLGVTDSPASVGTTELKFFNAEQKGSVCGEFIKVDFSAKEDVEEEKALRTLANVFKKLFSILRPNGKNEPNPNNNNHKEDHAMNDKQFAQLIEAVKGLDAKIDNHFSAKVETKEPENKPEEKKDEQPQSVTAEQFNQLLITVQALDKKFNELSQEQTTVPSGVPTVEKENVYSLNGYNIDLSKGF
Enzyme Length 298
Uniprot Accession Number P51719
Absorption
Active Site ACT_SITE 21; /evidence=ECO:0000250|UniProtKB:P25478; ACT_SITE 50; /evidence=ECO:0000250|UniProtKB:P25478; ACT_SITE 97; /evidence=ECO:0000250|UniProtKB:P25478
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Scaffolding protein and protease involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are cleaved by the viral protease activity. {ECO:0000250|UniProtKB:P25478}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (2); Compositional bias (1); Propeptide (1); Region (1); Site (1)
Keywords Hydrolase;Protease;Reference proteome;Serine protease;Viral capsid assembly;Viral capsid maturation;Viral release from host cell
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Autocleaves itself into an N-terminal fragment containing the protease activity, that remains in the capsid following maturation. {ECO:0000250|UniProtKB:P25478}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 33,703
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda